Data for: Why the lower reported prevalence of asthma in patients diagnosed with COVID-19 validates repurposing EDTA solutions to prevent and manage treat COVID-19 disease.
The NCBI pBlast tool was used to test the hypothesis that SARS-CoV-2 contains a calcium-dependent fusion domain(s) similar to those that were recently discovered in both Rubella and SARS-CoV-1. An Amino Acids comparison of the two relevant amino acid regions in S protein of SARS-CoV-1 representing fusion loop 1 (FL1 = Amino Acids 798- 819) and fusion loop 2 (FL2 = Amino Acids 835 -855) was conducted using the Protein Blast program from the National Center for Biotechnology Information. Specifically, Table 1 and Table 2 exhibit the data from the Protein Blast Alignment Tool data from the calcium binding fusion domains, labeled FL1 and FL2 respectively, that compare the spike proteins of COVID-19 (SARS-CoV-2) with SARS-COV and Rubella utilizing cited reference data; GenBank: QHD43416.1 (CoV-2), NCBI Reference Sequence: NP_828851.1(CoV-1), GenBank: ACN50046.1. (Rubella), GenBank: NP_828851(Human coronavirus229E) and GenBank: AD177360.1 (hemagglutinin [Influenza A virus (A/Boston/136/2009(H1N1))]). The results demonstrated a 100% and a 95% correspondence respectively between the postulated FL1 and FL2 domains in SARS-CoV-2 (COVID-19) compared to the known FL regions for SARS-CoV-1 described in 2017. Additionally, the less pathogenic Alpha coronavirus 229E (HCoV-229E) has a solitary FL2 domain and a reduced homology length compared to the SARS-CoV-2 (COVID-19) FL2. Similarly, amino acids 49 to 55 of the Rubella Virus membrane glycoprotein E2 virus also have a smaller, but significant homology with the FL2 domain. In contrast, the Influenza H1N1 hemagglutinin (HA) protein has no significant similarity to any of the CoV FL domains. The reduced homology of HCoV-229E’s single calcium-binding domain to SARS-CoV-2 suggests attenuation of HCoV-229E, which is consistent with HC0V-229E having crossed species barriers to infect humans decades or centuries ago.